› 1teh

X-ray diffraction
2.7Å resolution

STRUCTURE OF HUMAN LIVER CHICHI ALCOHOL DEHYDROGENASE (A GLUTATHIONE-DEPENDENT FORMALDEHYDE DEHYDROGENASE)

Released:
DOI: 10.2210/pdb1teh/pdb
PDB entry 1teh coloured by chain, front view.
PDB entry 1teh coloured by chain, side view.
PDB entry 1teh coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of human chi chi alcohol dehydrogenase: a glutathione-dependent formaldehyde dehydrogenase.
Yang ZN, Bosron WF, Hurley TD
J Mol Biol 265 330-43 (1997)
PMID: 9018047

Function and Biology Details

Reactions catalysed: 
A primary alcohol + NAD(+) = an aldehyde + NADH
S-(hydroxymethyl)glutathione + NAD(P)(+) = S-formylglutathione + NAD(P)H
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145918 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alcohol dehydrogenase class-3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 373 amino acids
Theoretical weight: 39.64 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P11766 (Residues: 2-374; Coverage: 100%)
Gene names: ADH5, ADHX, FDH
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 2 x NAD
1 bound ligand:
Ligand ZN 5 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: C2221
Unit cell:
a: 141.25Å b: 201.55Å c: 69.61Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.206 0.283

Quick links

Citations

6 review citations

Metabolic methanol: molecular pathways and physiological roles.
Dorokhov et al. (2015)
5 more

5 mentions without citation

Yeast alcohol dehydrogenase structure and catalysis.
Raj et al. (2014)
4 more